Evidence map›Paper›PMID 33314350›Full record

ReviewMolecular microbiology2021

The assembly of β-barrel membrane proteins by BAM and SAM.

Karl Lundquist, Evan Billings, Maxine Bi, James Wellnitz, Nicholas Noinaj

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Discovery and characterization of an anti-Frontiers in microbiology · 2026
    Article
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  7. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Karl LundquistDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA.ORCID 0000-0002-3418-8342
Evan BillingsDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA.
Maxine BiDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA.
James WellnitzDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA.
Nicholas NoinajDepartment of Biological Sciences, Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA.ORCID 0000-0001-6361-2336
Purdue University West Lafayette · US

Funding

Purdue University Molecular Biophysics Training ProgramT32GM132024 · NIGMS · PURDUE UNIVERSITY · PI Angeline Marie Lyon, John Tesmer · 2019 to 2026
$2.0M
Structural Characterization of the TOC Protein Translocon MachineryR01GM127896 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2018 to 2022
$1.5M
Unraveling the mechanism by which the BAM complex mediates OMP biogenesisR01GM127884 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2019 to 2022
$1.2M
Drug Discovery in Infectious Disease TrainingT32AI148103 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL, YEO, YOON · 2020 to 2024
$949k
NIAID NIH HHS T32 AI148103NIGMS NIH HHS R01 GM127884NIGMS NIH HHS R01 GM127896NIGMS NIH HHS T32 GM132024
6 · The paper itself

Abstract

Gram-negative bacteria, mitochondria, and chloroplasts all possess an outer membrane populated with a host of β-barrel outer-membrane proteins (βOMPs). These βOMPs play crucial roles in maintaining viability of their hosts, and therefore, it is essential to understand the biogenesis of this class of membrane proteins. In recent years, significant structural and functional advancements have been made toward elucidating this process, which is mediated by the β-barrel assembly machinery (BAM) in Gram-negative bacteria, and by the sorting and assembly machinery (SAM) in mitochondria. Structures of both BAM and SAM have now been reported, allowing a comparison and dissection of the two machineries, with other studies reporting on functional aspects of each. Together, these new insights provide compelling support for the proposed budding mechanism, where each nascent βOMP forms a hybrid-barrel intermediate with BAM/SAM in route to its biogenesis into the membrane. Here, we will review these recent studies and highlight their contributions toward understanding βOMP biogenesis in Gram-negative bacteria and in mitochondria. We will also weigh the evidence supporting each of the two leading mechanistic models for how BAM/SAM function, and offer an outlook on future studies within the field.

Indexed as

Protein FoldingAmino Acid MotifsBacterial Outer Membrane ProteinsChloroplastsGram-Negative BacteriaMitochondriaMitochondrial Membrane Transport ProteinsModels, MolecularMultiprotein ComplexesProtein ConformationBacterial Outer Membrane ProteinsMitochondrial Membrane Transport ProteinsMultiprotein Complexesenvelope biogenesisGram-negative bacterialateral gateouter membraneouter membrane proteinprotein foldingβ-barrel

Identifiers

PMID33314350
PMCPMC8608283
OpenAlexW3112423269

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.